|
Name |
Accession |
Description |
Interval |
E-value |
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
2-251 |
4.50e-156 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 433.66 E-value: 4.50e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDtLAAIPGSKGQYGYPFTVNTSVNEVVCHGWPSA 81
Cdd:COG0024 3 IKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRD-HGAIPAFLGYYGFPKSICTSVNEVVVHGIPSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 82 QqILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSV 161
Cdd:COG0024 82 R-VLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 162 VREYCGHGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTERG 241
Cdd:COG0024 161 VREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDG 240
|
250
....*....|
gi 489205359 242 CRVLTLRDEE 251
Cdd:COG0024 241 PEILTLPDGG 250
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
2-251 |
6.97e-149 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 415.69 E-value: 6.97e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDtLAAIPGSKGQYGYPFTVNTSVNEVVCHGWPSA 81
Cdd:PRK05716 5 IKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRD-QGAIPAPLGYHGFPKSICTSVNEVVCHGIPSD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 82 QqILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSV 161
Cdd:PRK05716 84 K-VLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 162 VREYCGHGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTERG 241
Cdd:PRK05716 163 VREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTEDG 242
|
250
....*....|
gi 489205359 242 CRVLTLRDEE 251
Cdd:PRK05716 243 PEILTLRPEE 252
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
8-247 |
3.00e-133 |
|
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Pssm-ID: 238519 [Multi-domain] Cd Length: 238 Bit Score: 375.68 E-value: 3.00e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 8 IQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDtLAAIPGSKGQYGYPFTVNTSVNEVVCHGWPSaQQILRD 87
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEE-HGAYPAPLGYYGFPKSICTSVNEVVCHGIPD-DRVLKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 88 GDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSVVREYCG 167
Cdd:cd01086 79 GDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 168 HGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTERGCRVLTL 247
Cdd:cd01086 159 HGIGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
2-248 |
3.90e-116 |
|
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine. [Protein fate, Protein modification and repair]
Pssm-ID: 129591 [Multi-domain] Cd Length: 247 Bit Score: 332.78 E-value: 3.90e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDTlAAIPGSKGQYGYPFTVNTSVNEVVCHGWPSa 81
Cdd:TIGR00500 3 LKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKH-GAKPAFLGYYGFPGSVCISVNEVVIHGIPD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 82 QQILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSV 161
Cdd:TIGR00500 81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 162 VREYCGHGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTERG 241
Cdd:TIGR00500 161 VREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNG 240
|
....*..
gi 489205359 242 CRVLTLR 248
Cdd:TIGR00500 241 PEILTER 247
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
9-239 |
2.15e-55 |
|
Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.
Pssm-ID: 459852 [Multi-domain] Cd Length: 208 Bit Score: 177.05 E-value: 2.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 9 QRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDTLAAipgskGQYGYPFTVNTSVNEVVCHGWPSAQQiLRDG 88
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA-----RGPAFPPIVASGPNAAIPHYIPNDRV-LKPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 89 DIVNVDVTVI-KDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYS-VVREYC 166
Cdd:pfam00557 75 DLVLIDVGAEyDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489205359 167 GHGIGRKMHEAPQVlhfGRAGAGARLKAGMTFTIEPMINqgghavklHKDGWTvttrdrrlSAQYEHTVLVTE 239
Cdd:pfam00557 155 GHGIGLEVHEGPYI---SRGGDDRVLEPGMVFTIEPGIY--------FIPGWG--------GVRIEDTVLVTE 208
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
2-251 |
4.50e-156 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 433.66 E-value: 4.50e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDtLAAIPGSKGQYGYPFTVNTSVNEVVCHGWPSA 81
Cdd:COG0024 3 IKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRD-HGAIPAFLGYYGFPKSICTSVNEVVVHGIPSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 82 QqILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSV 161
Cdd:COG0024 82 R-VLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 162 VREYCGHGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTERG 241
Cdd:COG0024 161 VREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDG 240
|
250
....*....|
gi 489205359 242 CRVLTLRDEE 251
Cdd:COG0024 241 PEILTLPDGG 250
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
2-251 |
6.97e-149 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 415.69 E-value: 6.97e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDtLAAIPGSKGQYGYPFTVNTSVNEVVCHGWPSA 81
Cdd:PRK05716 5 IKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRD-QGAIPAPLGYHGFPKSICTSVNEVVCHGIPSD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 82 QqILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSV 161
Cdd:PRK05716 84 K-VLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 162 VREYCGHGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTERG 241
Cdd:PRK05716 163 VREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTEDG 242
|
250
....*....|
gi 489205359 242 CRVLTLRDEE 251
Cdd:PRK05716 243 PEILTLRPEE 252
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
8-247 |
3.00e-133 |
|
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Pssm-ID: 238519 [Multi-domain] Cd Length: 238 Bit Score: 375.68 E-value: 3.00e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 8 IQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDtLAAIPGSKGQYGYPFTVNTSVNEVVCHGWPSaQQILRD 87
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEE-HGAYPAPLGYYGFPKSICTSVNEVVCHGIPD-DRVLKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 88 GDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSVVREYCG 167
Cdd:cd01086 79 GDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 168 HGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTERGCRVLTL 247
Cdd:cd01086 159 HGIGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
2-248 |
3.90e-116 |
|
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine. [Protein fate, Protein modification and repair]
Pssm-ID: 129591 [Multi-domain] Cd Length: 247 Bit Score: 332.78 E-value: 3.90e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDTlAAIPGSKGQYGYPFTVNTSVNEVVCHGWPSa 81
Cdd:TIGR00500 3 LKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKH-GAKPAFLGYYGFPGSVCISVNEVVIHGIPD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 82 QQILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSV 161
Cdd:TIGR00500 81 KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 162 VREYCGHGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTERG 241
Cdd:TIGR00500 161 VREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNG 240
|
....*..
gi 489205359 242 CRVLTLR 248
Cdd:TIGR00500 241 PEILTER 247
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
2-248 |
5.11e-109 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 314.85 E-value: 5.11e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDtLAAIPGSKGQYGYPFTVNTSVNEVVCHGWPSA 81
Cdd:PRK12896 10 IKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEE-HGAIPSPEGYYGFPGSTCISVNEEVAHGIPGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 82 QqILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSV 161
Cdd:PRK12896 89 R-VIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNGYSV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 162 VREYCGHGIGRKMHEAPQV-LHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTER 240
Cdd:PRK12896 168 VRDLTGHGVGRSLHEEPSViLTYTDPLPNRLLRPGMTLAVEPFLNLGAKDAETLDDGWTVVTPDKSLSAQFEHTVVVTRD 247
|
....*...
gi 489205359 241 GCRVLTLR 248
Cdd:PRK12896 248 GPEILTDR 255
|
|
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
2-248 |
5.34e-83 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 253.99 E-value: 5.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVdTLAAIPGSKGQYGYPFTVNTSVNEVVCHGWPSA 81
Cdd:PLN03158 137 IKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVHEATI-AAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 82 QQiLRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSV 161
Cdd:PLN03158 216 RK-LEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 162 VREYCGHGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTERG 241
Cdd:PLN03158 295 VKSYCGHGIGELFHCAPNIPHYARNKAVGVMKAGQVFTIEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTETG 374
|
....*..
gi 489205359 242 CRVLTLR 248
Cdd:PLN03158 375 VEVLTAR 381
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
1-249 |
4.89e-71 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 219.69 E-value: 4.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 1 MIKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFcERYIVDTLAAIPG--SKGQYGYPFTVNTSVNEVVCHGW 78
Cdd:PRK12318 42 IIKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDEL-SRELHKEYNAIPAplNYGSPPFPKTICTSLNEVICHGI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 79 PSaQQILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANG 158
Cdd:PRK12318 121 PN-DIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 159 YSVVREYCGHGIGRKMHEAPQVLHFgRAGAGARLKAGMTFTIEPMINQGG-HAVKLHKDGWTVTTRDRRLSAQYEHTVLV 237
Cdd:PRK12318 200 FSVVDQFVGHGVGIKFHENPYVPHH-RNSSKIPLAPGMIFTIEPMINVGKkEGVIDPINHWEARTCDNQPSAQWEHTILI 278
|
250
....*....|..
gi 489205359 238 TERGCRVLTLRD 249
Cdd:PRK12318 279 TETGYEILTLLD 290
|
|
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
2-246 |
3.57e-70 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 216.05 E-value: 3.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIvDTLAAIPGSKGQYGYPFTVNTSVNEVVCHGWPsA 81
Cdd:PRK12897 4 IKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYL-EKHGATSEQKGYNGYPYAICASVNDEMCHAFP-A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 82 QQILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSV 161
Cdd:PRK12897 82 DVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 162 VREYCGHGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAVKLHKDGWTVTTRDRRLSAQYEHTVLVTERG 241
Cdd:PRK12897 162 ARDFTGHGIGKEIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRYSKVDLNGWTARTMDGKLSAQYEHTIAITKDG 241
|
....*
gi 489205359 242 CRVLT 246
Cdd:PRK12897 242 PIILT 246
|
|
| PRK07281 |
PRK07281 |
methionyl aminopeptidase; |
2-252 |
1.21e-57 |
|
methionyl aminopeptidase;
Pssm-ID: 180918 Cd Length: 286 Bit Score: 185.44 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVD--TLAAIPGSKGQY-GYPFTVNTSVNEVVCHGW 78
Cdd:PRK07281 4 LKSAREIEAMDRAGDFLASIHIGLRDLIKPGVDMWEVEEYVRRRCKEenVLPLQIGVDGAMmDYPYATCCGLNDEVAHAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 79 PSaQQILRDGDIVNVDVTV------------------------IKDGYFG---DSSKMYRVGAIDRQAQKLLDVTRECLY 131
Cdd:PRK07281 84 PR-HYILKEGDLLKVDMVLsepldksivdvsklnfdnveqmkkYTESYRGglaDSCWAYAVGTPSDEVKNLMDVTKEAMY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 132 RAIRVVRPDATLGDIGHAIQSHAEANGYSVVREYCGHGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQGGHAV 211
Cdd:PRK07281 163 RGIEQAVVGNRIGDIGAAIQEYAESRGYGVVRDLVGHGVGPTMHEEPMVPNYGTAGRGLRLREGMVLTIEPMINTGTWEI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489205359 212 KLH-KDGWTVTTRDRRLSAQYEHTVLVTERGCRVLTLRDEER 252
Cdd:PRK07281 243 DTDmKTGWAHKTLDGGLSCQYEHQFVITKDGPVILTSQGEER 284
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
9-239 |
2.15e-55 |
|
Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.
Pssm-ID: 459852 [Multi-domain] Cd Length: 208 Bit Score: 177.05 E-value: 2.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 9 QRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDTLAAipgskGQYGYPFTVNTSVNEVVCHGWPSAQQiLRDG 88
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA-----RGPAFPPIVASGPNAAIPHYIPNDRV-LKPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 89 DIVNVDVTVI-KDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYS-VVREYC 166
Cdd:pfam00557 75 DLVLIDVGAEyDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489205359 167 GHGIGRKMHEAPQVlhfGRAGAGARLKAGMTFTIEPMINqgghavklHKDGWTvttrdrrlSAQYEHTVLVTE 239
Cdd:pfam00557 155 GHGIGLEVHEGPYI---SRGGDDRVLEPGMVFTIEPGIY--------FIPGWG--------GVRIEDTVLVTE 208
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
1-246 |
2.60e-36 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 130.32 E-value: 2.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 1 MIKSAEEIQRMSVAGALTAKVLEALDEVVRPGIStaeidrfcERYIVDTLAAIPGSKGQYGYPFTVNTSVNE--VVCHGW 78
Cdd:COG0006 72 AIKSPEEIELMRKAARIADAAHEAALAALRPGVT--------EREVAAELEAAMRRRGAEGPSFDTIVASGEnaAIPHYT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 79 PSAQQIlRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANG 158
Cdd:COG0006 144 PTDRPL-KPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 159 YsvvREY----CGHGIGRKMHEAPQVlhfgRAGAGARLKAGMTFTIEPMI-NQGGHAVKLhkdgwtvttrdrrlsaqyEH 233
Cdd:COG0006 223 Y---GEYfphgTGHGVGLDVHEGPQI----SPGNDRPLEPGMVFTIEPGIyIPGIGGVRI------------------ED 277
|
250
....*....|...
gi 489205359 234 TVLVTERGCRVLT 246
Cdd:COG0006 278 TVLVTEDGAEVLT 290
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
8-242 |
1.21e-34 |
|
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation.
Pssm-ID: 238514 [Multi-domain] Cd Length: 207 Bit Score: 123.72 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 8 IQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVdtlaaipgsKGQYGYPFTVNTSVNEV--VCHGWPSAQqIL 85
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALR---------AAGGYPAGPTIVGSGARtaLPHYRPDDR-RL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 86 RDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSVVR-E 164
Cdd:cd01066 71 QEGDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFgH 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489205359 165 YCGHGIGRKMHEAPqvlhFGRAGAGARLKAGMTFTIEPMINQGGhavklhkdgwtvttrdrRLSAQYEHTVLVTERGC 242
Cdd:cd01066 151 RTGHGIGLEIHEPP----VLKAGDDTVLEPGMVFAVEPGLYLPG-----------------GGGVRIEDTVLVTEDGP 207
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
1-207 |
2.51e-26 |
|
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. The role of this protein in general is to produce the mature amino end of cytosolic proteins by removing the N-terminal methionine. This model describes type II, among which the eukaryotic members typically have an N-terminal extension not present in archaeal members. It can act cotranslationally. The enzyme from rat has been shown to associate with translation initiation factor 2 (IF-2) and may have a role in translational regulation. [Protein fate, Protein modification and repair]
Pssm-ID: 129592 Cd Length: 295 Bit Score: 104.10 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 1 MIKSAEEIQRmsvAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDtLAAIPGskgqygypFTVNTSVNEVVCHGWPS 80
Cdd:TIGR00501 1 DIERAEKWIE---AGKIHSKVRREAADRIVPGVKLLEVAEFVENRIRE-LGAEPA--------FPCNISINECAAHFTPK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 81 A--QQILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAidrQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANG 158
Cdd:TIGR00501 69 AgdKTVFKDGDVVKLDLGAHVDGYIADTAITVDLGD---QYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIESYG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489205359 159 YSVVREYCGHGIGRKMHEAPQVLHFGRAGAGARLKAGMTFTIEPMINQG 207
Cdd:TIGR00501 146 VKPISNLTGHSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDG 194
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
14-246 |
2.79e-26 |
|
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Pssm-ID: 238521 [Multi-domain] Cd Length: 291 Bit Score: 103.87 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 14 AGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDtLAAIPGskgqygypFTVNTSVNEVVCHGWPSAQQ--ILRDGDIV 91
Cdd:cd01088 7 AGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRE-LGAGPA--------FPVNLSINECAAHYTPNAGDdtVLKEGDVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 92 NVDVTVIKDGYFGDSskmyrvgAI----DRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSVVREYCG 167
Cdd:cd01088 78 KLDFGAHVDGYIADS-------AFtvdfDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGFKPIRNLTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 168 HGIGRkmheapQVLHFG------RAGAGARLKAGMTFTIEPMINQGGHAVklHKDGWT--------VTTRDRR------- 226
Cdd:cd01088 151 HSIER------YRLHAGksipnvKGGEGTRLEEGDVYAIEPFATTGKGYV--HDGPECsiymlnrdKPLRLPRarklldv 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489205359 227 ------------------------------------------------LSAQYEHTVLVTERGCRVLT 246
Cdd:cd01088 223 iyenfgtlpfarrwldrlgetkllmalknlckagivypypvlkeisggYVAQFEHTIIVREDGKEVTT 290
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
8-242 |
1.15e-24 |
|
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse hydrolysis of Xaa-Pro dipeptides and/or release of any N-terminal amino acid, including proline, that is linked with proline.
Pssm-ID: 238525 [Multi-domain] Cd Length: 208 Bit Score: 97.58 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 8 IQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDtlaaipgsKGQYGYPFT--VNTSVNEVVCHGWPSAQqIL 85
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRK--------LGAEGPSFDtiVASGPNSALPHGVPSDR-KI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 86 RDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSvvrEY 165
Cdd:cd01092 72 EEGDLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYG---EY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 166 ----CGHGIGRKMHEAPQVlhfgRAGAGARLKAGMTFTIEPMI---NQGGhaVKLhkdgwtvttrdrrlsaqyEHTVLVT 238
Cdd:cd01092 149 fihrTGHGVGLEVHEAPYI----SPGSDDVLEEGMVFTIEPGIyipGKGG--VRI------------------EDDVLVT 204
|
....
gi 489205359 239 ERGC 242
Cdd:cd01092 205 EDGC 208
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
14-246 |
1.06e-11 |
|
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family members have been implicated in cell cycle control.
Pssm-ID: 238522 Cd Length: 228 Bit Score: 62.73 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 14 AGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDTLAAI-PGSKGQY-GYPFTVNTSVNEVVCHGWP---SAQQILRDG 88
Cdd:cd01089 7 AGQIANKVLKQVISLCVPGAKVVDLCEKGDKLILEELGKVyKKEKKLEkGIAFPTCISVNNCVCHFSPlksDATYTLKDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 89 DIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQ--KLLDV---TRECLYRAIRVVRPDATLGDIGHAIQSHAEANGYSVVR 163
Cdd:cd01089 87 DVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVtgKKADViaaAHYALEAALRLLRPGNQNSDITEAIQKVIVDYGCTPVE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 164 EYCGHgigrkmheapqvlhfgragagaRLKAGMTFtiepminqGGHAVKLHK-------DGWTV-TTRDRRLSAQYEHTV 235
Cdd:cd01089 167 GVLSH----------------------QLKRVVSS--------GEGKAKLVEcvkhgllFPYPVlYEKEGEVVAQFKLTV 216
|
250
....*....|.
gi 489205359 236 LVTERGCRVLT 246
Cdd:cd01089 217 LLTPNGVTVLT 227
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
4-201 |
2.23e-11 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 63.19 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 4 SAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIdrfCERyIVDTLAAIPGSKG-QYGYPFTVNTSVNEVVCHGWPSAQ 82
Cdd:PTZ00053 154 SEEQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDI---CER-IESKSRELIEADGlKCGWAFPTGCSLNHCAAHYTPNTG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 83 Q--ILRDGDIVNVDVTVIKDGYFGDSSkmYRVgAIDRQAQKLLDVTRECLYRAIRVVRPDATLGDIGHAIQ----SH-AE 155
Cdd:PTZ00053 230 DktVLTYDDVCKLDFGTHVNGRIIDCA--FTV-AFNPKYDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQevieSYeVE 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489205359 156 ANG--YSV--VREYCGHGIGrkmheaPQVLHFG------RAGAGARLKAGMTFTIE 201
Cdd:PTZ00053 307 IKGktYPIksIRNLNGHSIG------PYIIHGGksvpivKGGENTRMEEGELFAIE 356
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
2-245 |
1.13e-09 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 58.03 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIDRFCERYIVDTLAAipgskgqygypftvNTSVNEVVCHGWPSA 81
Cdd:PRK09795 127 IKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAE--------------KASFDTIVASGWRGA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 82 -------QQILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQK-----LLDVTRECLYRAIRVVRPDATLGDIGHA 149
Cdd:PRK09795 193 lphgkasDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAEShplfnVYQIVLQAQLAAISAIRPGVRCQQVDDA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 150 IQSHAEANGYSvvrEY----CGHGIGRKMHEAPQVlhfgRAGAGARLKAGMTFTIEPMI---NQGGhavklhkdgwtvtt 222
Cdd:PRK09795 273 ARRVITEAGYG---DYfghnTGHAIGIEVHEDPRF----SPRDTTTLQPGMLLTVEPGIylpGQGG-------------- 331
|
250 260
....*....|....*....|...
gi 489205359 223 rdrrlsAQYEHTVLVTERGCRVL 245
Cdd:PRK09795 332 ------VRIEDVVLVTPQGAEVL 348
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
8-246 |
6.51e-08 |
|
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro.
Pssm-ID: 238520 [Multi-domain] Cd Length: 243 Bit Score: 51.80 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 8 IQRMSVAGALTAKVLEALDEVVRPGIS----TAEIDRFCERYivdtlaaipgsKGQYGYPFTVNTSVNEVVCHgWPSAQQ 83
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMSeyelEAEFEYEFRSR-----------GARLAYSYIVAAGSNAAILH-YVHNDQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 84 ILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQAQK-----LLDVTREClyraIRVVRPDATLGDI-GHAIQSHAE-- 155
Cdd:cd01087 69 PLKDGDLVLIDAGAEYGGYASDITRTFPVNGKFTDEQRelyeaVLAAQKAA----IAACKPGVSYEDIhLLAHRVLAEgl 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 156 ------------ANGYSVVREYC----GHGIGRKMHEAPQVLHFGRAGAgaRLKAGMTFTIEP--MINQGGHAVKLHKDG 217
Cdd:cd01087 145 kelgilkgdvdeIVESGAYAKFFphglGHYLGLDVHDVGGYLRYLRRAR--PLEPGMVITIEPgiYFIPDLLDVPEYFRG 222
|
250 260
....*....|....*....|....*....
gi 489205359 218 WTVttrdrRLsaqyEHTVLVTERGCRVLT 246
Cdd:cd01087 223 GGI-----RI----EDDVLVTEDGPENLT 242
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
2-172 |
3.10e-06 |
|
42K curved DNA binding protein; Proteins identified by this model have been identified in a number of species as a nuclear (but not nucleolar) protein with a cell cycle dependence. Various names given to members of this family have included cell cycle protein p38-2G4, DNA-binding protein GBP16, and proliferation-associated protein 1. This protein is closely related to methionine aminopeptidase, a cobolt-binding protein. [Unknown function, General]
Pssm-ID: 273105 Cd Length: 390 Bit Score: 47.58 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 2 IKSAEEIQRMSVAGALTAKVLEALDEVVRPGISTAEIdrfCER---YIVDTLAAI--PGSKGQYGYPFTVNTSVNEVVCH 76
Cdd:TIGR00495 14 LSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDI---CEKgdaFIMEETAKIfkKEKEMEKGIAFPTCISVNNCVGH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 77 GWPSA---QQILRDGDIVNVDVTVIKDGYFGDSSKMYRVGAIDRQ--AQKLLDVTRE---CLYRAIRVVRPDATLGDIGH 148
Cdd:TIGR00495 91 FSPLKsdqDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEpvTGRKADVIAAahlAAEAALRLVKPGNTNTQVTE 170
|
170 180
....*....|....*....|....
gi 489205359 149 AIQSHAEANGYSVVREYCGHGIGR 172
Cdd:TIGR00495 171 AINKVAHSYGCTPVEGMLSHQLKQ 194
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
1-255 |
3.11e-05 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 44.72 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 1 MIKSAEEIQRMSVAGALTAKVLEALDEVVRPGIST----AEIDRFCERYivdtlaaipGSKgqygYPfTVNTSV----NE 72
Cdd:PRK10879 172 LFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEyqleGEIHHEFNRH---------GAR----YP-SYNTIVgsgeNG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 73 VVCHgWPSAQQILRDGDIVNVDVTVIKDGYFGDSSKMYRV-GAIDRQAQKLLDVTRECLYRAIRVVRPDATL-------- 143
Cdd:PRK10879 238 CILH-YTENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVnGKFTPAQREIYDIVLESLETSLRLYRPGTSIrevtgevv 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205359 144 --------------GDIGHAIQSHAEangysvvREYCGHG----IGRKMHEapqVLHFGrAGAGARLKAGMTFTIEPMIN 205
Cdd:PRK10879 317 rimvsglvklgilkGDVDQLIAENAH-------RPFFMHGlshwLGLDVHD---VGVYG-QDRSRILEPGMVLTVEPGLY 385
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250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489205359 206 QGGHAvklhkdgwTVTTRDRRLSAQYEHTVLVTERGCRVLT---LRD-EEREAL 255
Cdd:PRK10879 386 IAPDA--------DVPEQYRGIGIRIEDDIVITETGNENLTasvVKKpDEIEAL 431
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| APP |
cd01085 |
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ... |
167-202 |
8.20e-03 |
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X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline aminopeptidase, aminopeptidase P, and aminoacylproline aminopeptidase. Catalyses release of any N-terminal amino acid, including proline, that is linked with proline, even from a dipeptide or tripeptide.
Pssm-ID: 238518 [Multi-domain] Cd Length: 224 Bit Score: 36.77 E-value: 8.20e-03
10 20 30
....*....|....*....|....*....|....*...
gi 489205359 167 GHGIGR--KMHEAPQVLHFgrAGAGARLKAGMTFTIEP 202
Cdd:cd01085 161 GHGVGSflNVHEGPQSISP--APNNVPLKAGMILSNEP 196
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